Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and chi1 torsion angle preferences.
The behaviour of amino acid side-chains in proteins in solution has been characterised by analysing NMR 3JHalphaH beta coupling constants and crystallographic chi1 torsion angles. Side-chains both in the core of native folded proteins and in situations where there is an absence of close packing incl...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1998
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